Reviewed, UniProtKB/Swiss-Prot P30967 (PH4H_CHRVO)

Names and origin

Protein names

Recommended name:
    Phenylalanine-4-hydroxylase
      Short name=PAH
    EC=1.14.16.1
Alternative name(s):
    Phe-4-monooxygenase

Gene names

Name:	phhA
Ordered Locus Names:	CV_3180

Organism

Chromobacterium violaceum [Complete proteome] [HAMAP]

Taxonomic identifier

536 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin.
Cofactor	Fe2+ ion.
Pathway	Amino-acid degradation; L-phenylalanine degradation; acetoacetic acid and fumarate from L-phenylalanine: step 1/6.
Subunit structure	Monomer.
Sequence similarities	Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.
Sequence caution	The sequence AAA23115.1 differs from that shown. Reason: Frameshift at position 172.

Ontologies

Keywords
Biological process	Phenylalanine catabolism
Ligand	Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	L-phenylalanine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW phenylalanine 4-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 297

297

Phenylalanine-4-hydroxylase

PRO_0000205553

Sites

Metal binding

138

1

Iron

Metal binding

143

1

Iron

Metal binding

184

1

Iron

Experimental info

Sequence conflict

64

1

M → L Ref.1

Sequence conflict

64

1

M → L Ref.2

Sequence conflict

85

1

Q → E Ref.1

Sequence conflict

85

1

Q → E Ref.2

Sequence conflict

276

1

V → I Ref.1

Sequence conflict

276

1

V → I Ref.2

Sequence conflict

288

1

R → H Ref.1

Sequence conflict

288

1

R → H Ref.2

Secondary structure

1

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297

Helix Strand Turn

Details...

Helix

12 – 16

5

Turn

17 – 19

3

Turn

24 – 26

3

Helix

33 – 35

3

Helix

38 – 54

17

Turn

56 – 58

3

Helix

61 – 70

10

Beta strand

74 – 76

3

Helix

80 – 91

12

Beta strand

94 – 100

7

Helix

104 – 112

9

Beta strand

115 – 119

5

Beta strand

128 – 130

3

Helix

136 – 142

7

Helix

144 – 148

5

Helix

150 – 165

16

Helix

171 – 181

11

Turn

182 – 185

4

Beta strand

187 – 190

4

Beta strand

193 – 196

4

Helix

199 – 202

4

Helix

205 – 210

6

Beta strand

215 – 221

7

Helix

224 – 228

5

Beta strand

234 – 236

3

Beta strand

239 – 245

7

Helix

247 – 252

6

Helix

259 – 265

7

Sequences

	Sequence		Length	Mass (Da)
	P30967-1 [UniParc]. Last modified October 24, 2003. Version 4. Checksum: 6D29A04203E906FD	FASTA	297	33,616
	10 20 30 40 50 60 MNDRADFVVP DITTRKNVGL SHDANDFTLP QPLDRYSAED HATWATLYQR QCKLLPGRAC 70 80 90 100 110 120 DEFMEGLERL EVDADRVPDF NKLNQKLMAA TGWKIVAVPG LIPDDVFFEH LANRRFPVTW 130 140 150 160 170 180 WLREPHQLDY LQEPDVFHDL FGHVPLLINP VFADYLEAYG KGGVKAKALG ALPMLARLYW 190 200 210 220 230 240 YTVEFGLINT PAGMRIYGAG ILSSKSESIY CLDSASPNRV GFDLMRIMNT RYRIDTFQKT 250 260 270 280 290 YFVIDSFKQL FDATAPDFAP LYLQLADAQP WGAGDVAPDD LVLNAGDRQG WADTEDV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of Chromobacterium violaceum phenylalanine hydroxylase in Escherichia coli and comparison of amino acid sequence with mammalian aromatic amino acid hydroxylases." Onishi A., Liotta L.J., Benkovic S.J. J. Biol. Chem. 266:18454-18459(1991) [PubMed: 1655752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20. Strain: ATCC 12540 / NCTC 9695.
[2]	"Expression, isolation, and metal-dependent catalysis of phenylalanine hydroxylase from Chromobacterium violaceum." Volner A., Nersissian A.M., Abu-Omar M.M. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 12540 / NCTC 9695.
[3]	"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability." Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G. Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.
[4]	"Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates." Erlandsen H., Kim J.Y., Patch M.G., Han A., Volner A., Abu-Omar M.M., Stevens R.C. J. Mol. Biol. 320:645-661(2002) [PubMed: 12096915] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M55915 Genomic DNA. Translation: AAA23115.1. Frameshift.
AF146711 Genomic DNA. Translation: AAD37774.1.
AE016825 Genomic DNA. Translation: AAQ60846.1.

PIR

A40996.

RefSeq

NP_902850.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LTU	X-ray	1.74	A	1-297	[»]
1LTV	X-ray	2.00	A	1-297	[»]
1LTZ	X-ray	1.40	A	1-297	[»]

ModBase

Search...

Genome annotation databases

GeneID

2548525.

GenomeReviews

Gene locus CV_3180 in contig AE016825_GR.

KEGG

cvi:CV_3180.

NMPDR

fig|243365.1.peg.3180.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P30967.

OMA

P30967. FLARLYW.

Enzyme and pathway databases

BioCyc

CVIO243365:CV_3180-MON.
MetaCyc:MON-12067.

BRENDA

1.14.16.1. 415.

Family and domain databases

InterPro

IPR001273. ArAA_hydroxylase.
IPR018301. ArAA_hydroxylase_Fe/CU_BS.
IPR019774. Aromatic-AA_hydroxylase_C.
IPR005960. Phe-4-hydroxylase_mono.
[Graphical view]

Gene3D

G3DSA:1.10.800.10. Aaa_hydroxylase. 1 hit.

PANTHER

PTHR11473. Aaa_hydroxylase. 1 hit.

Pfam

PF00351. Biopterin_H. 1 hit.
[Graphical view]

PRINTS

PR00372. FYWHYDRXLASE.

ProDom

PD002559. Aaa_hydroxylase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01267. Phe4hydrox_mono. 1 hit.

PROSITE

PS00367. BIOPTERIN_HYDROXYL. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PH4H_CHRVO

Accession

Primary (citable) accession number: P30967
Secondary accession number(s): Q9R634, Q9XC88

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 24, 2003
Last modified:	June 16, 2009
This is version 93 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)